Document Detail


Antibodies to synthetic peptides corresponding to variable-region first-framework segments of T cell receptor. Detection of T cell products and cross-reactions with classical immunoglobulins.
MedLine Citation:
PMID:  2471756     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Recent studies at the gene level have shown that T cells express rearranged genes for four types of T cell receptors that are strongly homologous to classical immunoglobulins in the joining region and in the framework 1 (Fr1) and 3 segments of the variable region. Based upon the homologies in gene sequence, it follows that the gene products would show similarities in amino acid sequence and in the folding of the proteins so that cross-reactivities in antigenic determinants would be expected between variable regions of the T cell receptors and classical immunoglobulins. We have synthesized peptides corresponding to predicted protein sequences of the Fr1 residues of T cell receptor alpha, beta- and gamma-chains and have produced antibodies in rabbits against these synthetic peptides. Use of antisera and affinity-purified antipeptide antibodies indicated that high-titer antibodies could be raised that were specific for individual Fr1 peptides. Cross-reactions among Fr1 peptides of T cell receptors and immunoglobulin light chains were observed. In addition, some rabbit antisera raised against classical polyclonal immunoglobulins or affinity-purified immunoglobulin-like T cell receptors were found to exhibit binding activity against Fr1 peptides of T cell receptor beta- and gamma-chains. The sequence homology, although real among the Fr1 of T cell receptors and immunoglobulin light chains, is moderate and the antigenic cross-reaction must reflect the configuration and types of amino acids present. The development of antipeptide antibodies holds promise for the characterization of T cell receptors of various T cell sources and also offers a new means for the identification of molecules related to rearranging immunoglobulins.
Authors:
C R Ross; R A Hubbard; S F Schluter; A Diamanduros; A C Wang; J J Marchalonis
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Immunologic research     Volume:  8     ISSN:  0257-277X     ISO Abbreviation:  Immunol. Res.     Publication Date:  1989  
Date Detail:
Created Date:  1989-07-27     Completed Date:  1989-07-27     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8611087     Medline TA:  Immunol Res     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  81-97     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston.
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MeSH Terms
Descriptor/Qualifier:
Animals
Antibodies / immunology*
Cross Reactions
Epitopes / analysis*,  immunology
Humans
Immunoglobulin Fragments / immunology
Immunoglobulin Variable Region / immunology*
Mice
Peptides / immunology
Rabbits
Receptors, Antigen, T-Cell / analysis*,  immunology
Grant Support
ID/Acronym/Agency:
CA 34900/CA/NCI NIH HHS; CA 42049/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Antibodies; 0/Epitopes; 0/Immunoglobulin Fragments; 0/Immunoglobulin Variable Region; 0/Peptides; 0/Receptors, Antigen, T-Cell

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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